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EF手：修订间差异

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{{Pfam_box
#重定向 [[基尔德森林]]
| Symbol = efhand
| Name = EF手
| image = PDB_1osa_EBI.jpg
| width =
| caption =重组的{{le|第四双小核草履虫|Paramecium tetraurelia}}[[钙调蛋白]]结构<ref name="pmid15299476">{{cite journal |author=Ban C, Ramakrishnan B, Ling KY, Kung C, Sundaralingam M |title=Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 A resolution |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=50 |issue=Pt 1 |pages=50–63 |year=1994 |month=January |pmid=15299476 |doi=10.1107/S0907444993007991 |url=}}</ref>
| Pfam= PF00036
| PROSITE=PDOC00018
| InterPro= IPR002048
| SMART=
| SCOP = 1osa
| TCDB =
| OPM family=
| OPM protein= 1djx
| PDB=
{{PDB3|1s6j}}A:375-402 {{PDB3|1s6i}}A:375-403 {{PDB3|1m39}}A:141-169
{{PDB3|2a4j}}A:141-169 {{PDB3|1oqp}}A:138-166 {{PDB3|2bbn}}A:121-148
{{PDB3|2bkh}}B:121-148 {{PDB3|1mxe}}A:121-148 {{PDB3|4cln}} :121-148
{{PDB3|2bbm}}A:121-148 {{PDB3|1cdm}}A:121-146 {{PDB3|1lin}} :121-148
{{PDB3|2bki}}B:121-148 {{PDB3|1ooj}}A:121-148 {{PDB3|1osa}} :121-148
{{PDB3|1clm}} :121-147 {{PDB3|1n0y}}B:121-148 {{PDB3|1exr}}A:121-148
{{PDB3|1rfj}}A:121-149 {{PDB3|1ggz}}A:121-148 {{PDB3|1ak8}} :48-75
{{PDB3|1sw8}}A:48-76 {{PDB3|1j7o}}A:48-76 {{PDB3|1f70}}A:48-76
{{PDB3|1r2u}}A:56-84 {{PDB3|1r6p}}A:56-84 {{PDB3|1j1e}}A:56-84
}}

{{translating|[[:en:EF hand]]|time=2014-01-06|tpercent=4}}
The '''EF hand''' is a [[helix-loop-helix]] [[结构域]]或[[结构基序]] found in a large [[protein family|family]] of calcium-binding [[protein]]s.

The EF-hand motif contains a helix-loop-helix topology, much like the spread thumb and forefinger of the human hand, in which the Ca<sup>2+</sup> ions are coordinated by ligands within the loop. The [[Structural_motif#Structural_motifs_in_proteins|motif]] takes its name from traditional nomenclature used in describing the protein [[parvalbumin]], which contains three such motifs and is probably involved in [[muscle]] relaxation via its calcium-binding activity.

It consists of two [[alpha helix|alpha helices]] linked by a short loop region (usually about 12 [[amino acid]]s) that usually binds [[calcium]] ions. EF-hands also appear in each [[structural domain]] of the [[cell signaling|signaling protein]] [[calmodulin]] and in the muscle protein [[troponin-C]].

== 钙离子结合位点 ==
[[Image:EF hand.jpg|thumb|left|180px|EF-hand Ca<sup>2+</sup> binding motif. Image:EF-hand-prediction.jpg|thumb|180px|EF-hand Ca<sup>2+</sup> binding motif.]]
* The calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X and -Z. The invariant Glu or Asp at position 12 provides two oxygens for liganding Ca (bidentate ligand).
* The calcium ion is bound by both [[peptide bond|protein backbone]] atoms and by amino acid [[side chain]]s, specifically those of the acidic amino acid residues [[aspartate]] and [[glutamate]]. These residues are negatively charged and will make a charge-interaction with the positively charged calcium ion. The EF hand motif was among the first structural motifs whose sequence requirements were analyzed in detail. Five of the loop residues bind calcium and thus have a strong preference for [[oxygen]]-containing side chains, especially aspartate and glutamate. The sixth residue in the loop is necessarily [[glycine]] due to the conformational requirements of the backbone. The remaining residues are typically [[hydrophobic]] and form a [[hydrophobic core]] that binds and stabilizes the two helices.
* Upon binding to Ca<sup>2+</sup>, this motif may undergo conformational changes that enable Ca<sup>2+</sup>-regulated functions as seen in Ca<sup>2+</sup> effectors such as calmodulin (CaM) and troponin C (TnC) and Ca<sup>2+</sup> buffers such as calreticulin and calbindin D9k. While the majority of the known EF-hand Calcium-binding proteins (CaBPs) contain paired EF-hand motifs, CaBP’s with single EF hands have also been discovered in both bacteria and eukaryotes. In addition, “EF-hand-like motifs” have been found in a number of bacteria. Although the coordination properties remain similar with the canonical 29-residue helix-loop-helix EF-hand motif, the EF-hand-like motifs differ from EF-hands in that they contain deviations in the secondary structure of the flanking sequences and/or variation in the length of the Ca<sup>2+</sup>-coordinating loop.

== Prediction ==
[[Image:EF-hand-prediction.jpg|thumb|180px|Summary of motif signatures used for prediction of EF-hands.]]

* Pattern (motif signature) search is one of the most straightforward ways to predict continuous EF-hand Ca<sup>2+</sup>-binding sites in proteins. Based on the sequence alignment results of canonical EF-hand motifs, especially the conserved side chains directly involved in Ca<sup>2+</sup> binding, a pattern {{PROSITE|PS00018}} has been generated to predict canonical EF-hand sites. A prediction servers may be found in the external links section.

== 分类 ==
* Since the delineation of the EF-hand motif in 1973, the family of EF-hand proteins has expanded to include at least 66 subfamilies thus far. EF-hand motifs are divided into two major groups:
** '''Canonical EF-hands''' as seen in calmodulin (CaM) and the prokaryotic CaM-like protein calerythrin. The 12-residue canonical EF-hand loop binds Ca<sup>2+</sup> mainly via sidechain carboxylates or carbonyls (loop sequence positions 1, 3, 5, 12). The residue at the –X axis coordinates the Ca<sup>2+</sup> ion through a bridged water molecule. The EF-hand loop has a bidentate ligand (Glu or Asp) at axis –Z.
** '''Pseudo EF-hands''' exclusively found in the N-termini of S100 and S100-like proteins. The 14-residue pseudo EF-hand loop chelates Ca<sup>2+</sup> primarily via backbone carbonyls (positions 1, 4, 6, 9).
Additional points:
[[Image:EFhandtree.jpg|thumb|left|Phylogenetic tree of the EF-hand protein family.]]
* EF-hand-like proteins with diversified flanking structural elements around the Ca<sup>2+</sup>-binding loop have been reported in bacteria and viruses. These prokaryotic EF-hand-like proteins are widely implicated in Ca<sup>2+</sup> signaling and homeostasis in bacteria. They contain flexible lengths of Ca<sup>2+</sup>-binding loops that differ from the EF-hand motifs. However, their coordination properties resemble classical EF-hand motifs.
** For example, the semi-continuous Ca<sup>2+</sup>-binding site in D-galactose-binding protein (GBP) contains a nine-residue loop. The Ca<sup>2+</sup> ion is coordinated by seven protein oxygen atoms, five of which are from the loop mimicking the canonical EF-loop whereas the other two are from the carboxylate group of a distant Glu.
** Another example is a novel domain named Excalibur (extracellular Ca<sup>2+</sup>-binding region) isolated from ''Bacillus subtilis''. This domain has a conserved 10-residue Ca<sup>2+</sup>-binding loop strikingly similar to the canonical 12-residue EF-hand loop.
** The diversity of the structure of the flanking region is illustrated by the discovery of EF-hand-like domains in bacterial proteins. For example, a helix-loop-strand instead of the helix-loop-helix structure is in periplasmic galactose-binding protein (''[[Salmonella typhimurium]]'', {{PDB|1gcg}}) or alginate-binding protein (''[[Sphingomonas]] sp''., {{PDB2|1kwh}}); the entering helix is missing in protective antigen (''[[Bacillus anthracis]]'', {{PDB2|1acc}}) or dockerin (''[[Clostridium thermocellum]]'', {{PDB2|1daq}}).
*Among all the structures reported to date, the majority of EF-hand motifs are paired either between two canonical or one pseudo and one canonical motifs. For proteins with odd numbers of EF-hands, such as the penta-EF-hand calpain, EF-hand motifs were coupled through homo- or hetero-dimerization. The recently-identified EF-hand containing ER Ca<sup>2+</sup> sensor protein, stromal interaction molecule 1 and 2 (STIM1, STIM2), has been shown to contain a Ca<sup>2+</sup>-binding canonical EF-hand motif that pairs with an immediate, downstream atypical "hidden" non-Ca<sup>2+</sup>-binding EF-hand. Single EF-hand motifs can serve as protein-docking modules: for example, the single EF hand in the NKD1 and NKD2 proteins binds the Dishevelled (DVL1, DVL2, DVL3) proteins.
* Functionally, the EF-hands can be divided into two classes: 1) signaling proteins and 2) buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.

=== 亚族 ===
* EPS15 homology (EH) domain – {{InterPro|IPR000261}}

=== 例子 ===
Humans proteins containing this domain include:
* {{le|α-辅肌动蛋白1|ACTN1|ACTN1}}、{{le|α-辅肌动蛋白2|ACTN2|ACTN2}}、[[α-辅肌动蛋白3|ACTN3]]、{{le|α-辅肌动蛋白4|ACTN4|ACTN4}}、[[APBA2BP]]; [[AYTL1]]; [[AYTL2]]
* [[C14orf143]]; [[CABP1]]; [[CABP2]]; [[CABP3]]; [[CABP4]]; [[CABP5]]; [[CABP7]]; [[CALB1]]; [[CALB2]]; [[CALM2]]; [[CALM3]]; [[CALML3]]; [[CALML4]]; [[CALML5]]; [[CALML6]]; [[CALN1]]; [[CALU]]; [[CAPN1]]; [[CAPN11]]; [[CAPN2]]; [[CAPN3]]; [[CAPN9]]; [[CAPNS1]]; [[CAPNS2]]; [[CAPS (gene)|CAPS]]; [[CAPS2]]; [[CAPSL]]; [[CBARA1]]; [[CETN1]]; [[CETN2]]; [[CETN3]]; [[CHP (gene)|CHP]]; [[CHP2]]; [[CIB1]]; [[CIB2]]; [[CIB3]]; [[CIB4]]; [[CRNN]]
* [[DGKA]]; [[DGKB]]; [[DGKG]]; [[Dystonin|DST]]; [[DUOX1]]; [[DUOX2]]
* [[EFCAB1]]; [[EFCAB2]]; [[EFCAB4A]]; [[EFCAB4B]]; [[EFCAB6]]; [[EFCBP1]]; [[EFCBP2]]; [[EFHA1]]; [[EFHA2]]; [[EFHB]]; [[EFHC1]]; [[EFHD1]]; [[EFHD2]]; [[EPS15]]; [[EPS15L1]]
* [[FKBP10]]; [[FKBP14]]; [[FKBP7]]; [[FKBP9]]; [[FKBP9L]]; [[FREQ]]; [[FSTL1]]; [[FSTL5]]
* [[GCA (gene)|GCA]]; [[GPD2]]; [[GUCA1A]]; [[GUCA1B]]; [[GUCA1C]]
* [[hippocalcin]]; [[HPCAL1]]; [[HPCAL4]]; [[HZGJ]]
* [[IFPS]]; [[ITSN1]]; [[ITSN2]]; [[KCNIP1]]; [[KCNIP2]]; [[KCNIP3]]; [[KCNIP4]]; [[KIAA1799]]
* [[LCP1]]
* [[MACF1]]; [[MRLC2]]; [[MRLC3]]; [[MST133]]; [[MYL1]]; [[MYL2]]; [[MYL5]]; [[MYL6B]]; [[MYL7]]; [[MYL9]]; [[MYLC2PL]]; [[MYLPF]]
* [[NCALD]]; [[NIN (gene)|NIN]]; [[NKD1]]; [[NKD2]]; [[NINL|NLP]]; [[NOX5]]; [[NUCB1]]; [[NUCB2]]
* [[OCM (gene)|OCM]]
* [[PDCD6]]; [[PEF1]]; [[PKD2]]; [[PLCD1]]; [[PLCD4]]; [[PLCH1]]; [[PLCH2]]; [[PLS1]]; [[PLS3]]; [[PP1187]]; [[PPEF1]]; [[PPEF2]]; [[PPP3R1]]; [[PPP3R2]]; [[PRKCSH]]; [[PVALB]]
* [[RAB11FIP3]]; [[RASEF]]; [[RASGRP]]; [[RASGRP1]]; [[RASGRP2]]; [[RASGRP3]]; [[RCN1]]; [[RCN2]]; [[RCN3]]; [[RCV1]]; [[RCVRN]]; [[REPS1]]; [[RHBDL3]]; [[RHOT1]]; [[RHOT2]]; [[RPTN]]; [[RYR2]]; [[RYR3]]
* [[S100A1]]; [[S100A11]]; [[S100A12]]; [[S100A6]]; [[S100A8]]; [[S100A9]]; [[S100B]]; [[S100G]]; [[S100Z]]; [[SCAMC-2]]; [[SCGN]]; [[SCN5A]]; [[SDF4]]; [[SLC25A12]]; [[SLC25A13]]; [[SLC25A23]]; [[SLC25A24]]; [[SLC25A25]]; [[SPATA21]]; [[SPTA1]]; [[SPTAN1]]; [[SRI (gene)|SRI]]
* [[TBC1D9]]; [[TBC1D9B]]; [[TCHH]]; [[TESC (gene)|TESC]]; [[TNNC1]]; [[TNNC2]]
* [[USP32]]
* [[VSNL1]]
* [[ZZEF1]]

== 另见 ==
* Another distinct calcium-binding motif composed of alpha helices is the [[dockerin|dockerin domain]].

== 参考文献 ==
{{Reflist}}

== 延伸阅读 ==
{{refbegin | 2}}
* {{Cite book | author=Branden C, Tooze J | title = Introduction to Protein Structure | date=1999 | publisher = Garland Pub. | location = New York | isbn = 0-8153-2305-0 | chapter = Chapter 2: Motifs of protein structure | pages = 24–25}}
* {{cite journal | author = Nakayama S, Kretsinger RH | title = Evolution of the EF-hand family of proteins | journal = Annu Rev Biophys Biomol Struct | volume = 23 | issue = | pages = 473–507 | year = 1994 | pmid = 7919790 | doi = 10.1146/annurev.bb.23.060194.002353 | url = }}
* {{cite journal | author = Zhou Y, Yang W, Kirberger M, Lee HW, Ayalasomayajula G, Yang JJ | title = Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins | journal = Proteins | volume = 65 | issue = 3 | pages = 643–55 | year = 2006 | month = November | pmid = 16981205 | doi = 10.1002/prot.21139 | url = }}
* {{cite journal | author = Zhou Y, Frey TK, Yang JJ | title = Viral calciomics: interplays between Ca2+ and virus | journal = Cell Calcium | volume = 46 | issue = 1 | pages = 1–17 | year = 2009 | month = July | pmid = 19535138 | doi = 10.1016/j.ceca.2009.05.005 | url = }}
* {{cite journal | author = Nakayama S, Moncrief ND, Kretsinger RH | title = Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories | journal = J. Mol. Evol. | volume = 34 | issue = 5 | pages = 416–48 | year = 1992 | month = May | pmid = 1602495 | doi = 10.1007/BF00162998| url = }}
* {{cite journal | author = Hogue CW, MacManus JP, Banville D, Szabo AG | title = Comparison of terbium (III) luminescence enhancement in mutants of EF hand calcium binding proteins | journal = J. Biol. Chem. | volume = 267 | issue = 19 | pages = 13340–7 | year = 1992 | month = July | pmid = 1618836 | doi = | url = }}
* {{cite journal | author = Bairoch A, Cox JA | title = EF-hand motifs in inositol phospholipid-specific phospholipase C | journal = FEBS Lett. | volume = 269 | issue = 2 | pages = 454–6 | year = 1990 | month = September | pmid = 2401372 | doi = 10.1016/0014-5793(90)81214-9| url = }}
* {{cite journal | author = Finn BE, Forsén S | title = The evolving model of calmodulin structure, function and activation | journal = Structure | volume = 3 | issue = 1 | pages = 7–11 | year = 1995 | month = January | pmid = 7743133 | doi = 10.1016/S0969-2126(01)00130-7| url = }}
* {{cite journal | author = Stathopulos PB, Zheng L, Li GY, Plevin MJ, Ikura M | title = Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry | journal = Cell | volume = 135 | issue = 1 | pages = 110–22 | year = 2008 | month = October | pmid = 18854159 | doi = 10.1016/j.cell.2008.08.006 | url = }}
* {{cite journal | author = Nelson MR, Thulin E, Fagan PA, Forsén S, Chazin WJ | title = The EF-hand domain: a globally cooperative structural unit | journal = Protein Sci. | volume = 11 | issue = 2 | pages = 198–205 | year = 2002 | month = February | pmid = 11790829 | pmc = 2373453 | doi = 10.1110/ps.33302 | url = }}
{{refend}}

==外部链接==
* {{cite web | author = Nelson M, Chazin W | title = EF-Hand Calcium-Binding Proteins Data Library | url = http://structbio.vanderbilt.edu/cabp_database/| date = | work = | publisher = Vanderbilt University | accessdate = 2009-08-29 | quote = }}
* {{cite web | author = Haiech J | title = EF-hand protein database (EF-handome) | url = http://www.ulb.ac.be/assoc/ecs/ | date = | work = | publisher = European Calcium Society and the Université Libre de Bruxelles | accessdate = 2009-08-29 | quote = upon request to haiech@pharma.u-strasbg.fr }}
* {{cite web | author = Yang J | title = Calciomics | url = http://chemistry.gsu.edu/faculty/Yang/Calciomics.htm | date = | work = | publisher = Georgia State University | accessdate = 2009-08-29 | quote = prediction server for EF-hand calcium binding proteins }}
{{Protein secondary structure}}
{{Calcium signaling}}
[[Category:蛋白质结构模体]]
[[Category:蛋白质域]]
[[Category:外周膜蛋白]]

2014年1月6日 (一) 07:27的版本

EF手
鑑定
標誌efhand
PfamPF00036（旧版）
InterPro（英语：InterPro）IPR002048
PROSITE（英语：PROSITE）PDOC00018
SCOP（英语：Structural Classification of Proteins）1osa / SUPFAM
OPM（英语：Orientations of Proteins in Membranes database）蛋白1djx

The EF hand is a helix-loop-helix 结构域或结构基序 found in a large family of calcium-binding proteins.

The EF-hand motif contains a helix-loop-helix topology, much like the spread thumb and forefinger of the human hand, in which the Ca2+ ions are coordinated by ligands within the loop. The motif takes its name from traditional nomenclature used in describing the protein parvalbumin, which contains three such motifs and is probably involved in muscle relaxation via its calcium-binding activity.

It consists of two alpha helices linked by a short loop region (usually about 12 amino acids) that usually binds calcium ions. EF-hands also appear in each structural domain of the signaling protein calmodulin and in the muscle protein troponin-C.

钙离子结合位点

EF-hand Ca2+ binding motif.
  • The calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X and -Z. The invariant Glu or Asp at position 12 provides two oxygens for liganding Ca (bidentate ligand).
  • The calcium ion is bound by both protein backbone atoms and by amino acid side chains, specifically those of the acidic amino acid residues aspartate and glutamate. These residues are negatively charged and will make a charge-interaction with the positively charged calcium ion. The EF hand motif was among the first structural motifs whose sequence requirements were analyzed in detail. Five of the loop residues bind calcium and thus have a strong preference for oxygen-containing side chains, especially aspartate and glutamate. The sixth residue in the loop is necessarily glycine due to the conformational requirements of the backbone. The remaining residues are typically hydrophobic and form a hydrophobic core that binds and stabilizes the two helices.
  • Upon binding to Ca2+, this motif may undergo conformational changes that enable Ca2+-regulated functions as seen in Ca2+ effectors such as calmodulin (CaM) and troponin C (TnC) and Ca2+ buffers such as calreticulin and calbindin D9k. While the majority of the known EF-hand Calcium-binding proteins (CaBPs) contain paired EF-hand motifs, CaBP’s with single EF hands have also been discovered in both bacteria and eukaryotes. In addition, “EF-hand-like motifs” have been found in a number of bacteria. Although the coordination properties remain similar with the canonical 29-residue helix-loop-helix EF-hand motif, the EF-hand-like motifs differ from EF-hands in that they contain deviations in the secondary structure of the flanking sequences and/or variation in the length of the Ca2+-coordinating loop.

Prediction

Summary of motif signatures used for prediction of EF-hands.
  • Pattern (motif signature) search is one of the most straightforward ways to predict continuous EF-hand Ca2+-binding sites in proteins. Based on the sequence alignment results of canonical EF-hand motifs, especially the conserved side chains directly involved in Ca2+ binding, a pattern Template:PROSITE has been generated to predict canonical EF-hand sites. A prediction servers may be found in the external links section.

分类

  • Since the delineation of the EF-hand motif in 1973, the family of EF-hand proteins has expanded to include at least 66 subfamilies thus far. EF-hand motifs are divided into two major groups:
    • Canonical EF-hands as seen in calmodulin (CaM) and the prokaryotic CaM-like protein calerythrin. The 12-residue canonical EF-hand loop binds Ca2+ mainly via sidechain carboxylates or carbonyls (loop sequence positions 1, 3, 5, 12). The residue at the –X axis coordinates the Ca2+ ion through a bridged water molecule. The EF-hand loop has a bidentate ligand (Glu or Asp) at axis –Z.
    • Pseudo EF-hands exclusively found in the N-termini of S100 and S100-like proteins. The 14-residue pseudo EF-hand loop chelates Ca2+ primarily via backbone carbonyls (positions 1, 4, 6, 9).

Additional points:

Phylogenetic tree of the EF-hand protein family.
  • EF-hand-like proteins with diversified flanking structural elements around the Ca2+-binding loop have been reported in bacteria and viruses. These prokaryotic EF-hand-like proteins are widely implicated in Ca2+ signaling and homeostasis in bacteria. They contain flexible lengths of Ca2+-binding loops that differ from the EF-hand motifs. However, their coordination properties resemble classical EF-hand motifs.
    • For example, the semi-continuous Ca2+-binding site in D-galactose-binding protein (GBP) contains a nine-residue loop. The Ca2+ ion is coordinated by seven protein oxygen atoms, five of which are from the loop mimicking the canonical EF-loop whereas the other two are from the carboxylate group of a distant Glu.
    • Another example is a novel domain named Excalibur (extracellular Ca2+-binding region) isolated from Bacillus subtilis. This domain has a conserved 10-residue Ca2+-binding loop strikingly similar to the canonical 12-residue EF-hand loop.
    • The diversity of the structure of the flanking region is illustrated by the discovery of EF-hand-like domains in bacterial proteins. For example, a helix-loop-strand instead of the helix-loop-helix structure is in periplasmic galactose-binding protein (Salmonella typhimurium, PDB 1gcg) or alginate-binding protein (Sphingomonas sp., 1kwh); the entering helix is missing in protective antigen (Bacillus anthracis, 1acc) or dockerin (Clostridium thermocellum, 1daq).
  • Among all the structures reported to date, the majority of EF-hand motifs are paired either between two canonical or one pseudo and one canonical motifs. For proteins with odd numbers of EF-hands, such as the penta-EF-hand calpain, EF-hand motifs were coupled through homo- or hetero-dimerization. The recently-identified EF-hand containing ER Ca2+ sensor protein, stromal interaction molecule 1 and 2 (STIM1, STIM2), has been shown to contain a Ca2+-binding canonical EF-hand motif that pairs with an immediate, downstream atypical "hidden" non-Ca2+-binding EF-hand. Single EF-hand motifs can serve as protein-docking modules: for example, the single EF hand in the NKD1 and NKD2 proteins binds the Dishevelled (DVL1, DVL2, DVL3) proteins.
  • Functionally, the EF-hands can be divided into two classes: 1) signaling proteins and 2) buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.

亚族

例子

Humans proteins containing this domain include:

另见

  • Another distinct calcium-binding motif composed of alpha helices is the dockerin domain.

参考文献

  1. ^ Ban C, Ramakrishnan B, Ling KY, Kung C, Sundaralingam M. Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 A resolution. Acta Crystallogr. D Biol. Crystallogr. 1994, 50 (Pt 1): 50–63. PMID 15299476. doi:10.1107/S0907444993007991.  已忽略未知参数|month=（建议使用|date=） (帮助)

延伸阅读

  • Branden C, Tooze J. Chapter 2: Motifs of protein structure. Introduction to Protein Structure. New York: Garland Pub. 1999: 24–25. ISBN 0-8153-2305-0. 
  • Nakayama S, Kretsinger RH. Evolution of the EF-hand family of proteins. Annu Rev Biophys Biomol Struct. 1994, 23: 473–507. PMID 7919790. doi:10.1146/annurev.bb.23.060194.002353. 
  • Zhou Y, Yang W, Kirberger M, Lee HW, Ayalasomayajula G, Yang JJ. Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins. Proteins. 2006, 65 (3): 643–55. PMID 16981205. doi:10.1002/prot.21139.  已忽略未知参数|month=（建议使用|date=） (帮助)
  • Zhou Y, Frey TK, Yang JJ. Viral calciomics: interplays between Ca2+ and virus. Cell Calcium. 2009, 46 (1): 1–17. PMID 19535138. doi:10.1016/j.ceca.2009.05.005.  已忽略未知参数|month=（建议使用|date=） (帮助)
  • Nakayama S, Moncrief ND, Kretsinger RH. Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories. J. Mol. Evol. 1992, 34 (5): 416–48. PMID 1602495. doi:10.1007/BF00162998.  已忽略未知参数|month=（建议使用|date=） (帮助)
  • Hogue CW, MacManus JP, Banville D, Szabo AG. Comparison of terbium (III) luminescence enhancement in mutants of EF hand calcium binding proteins. J. Biol. Chem. 1992, 267 (19): 13340–7. PMID 1618836.  已忽略未知参数|month=（建议使用|date=） (帮助)
  • Bairoch A, Cox JA. EF-hand motifs in inositol phospholipid-specific phospholipase C. FEBS Lett. 1990, 269 (2): 454–6. PMID 2401372. doi:10.1016/0014-5793(90)81214-9.  已忽略未知参数|month=（建议使用|date=） (帮助)
  • Finn BE, Forsén S. The evolving model of calmodulin structure, function and activation. Structure. 1995, 3 (1): 7–11. PMID 7743133. doi:10.1016/S0969-2126(01)00130-7.  已忽略未知参数|month=（建议使用|date=） (帮助)
  • Stathopulos PB, Zheng L, Li GY, Plevin MJ, Ikura M. Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry. Cell. 2008, 135 (1): 110–22. PMID 18854159. doi:10.1016/j.cell.2008.08.006.  已忽略未知参数|month=（建议使用|date=） (帮助)
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外部链接

蛋白质二级结构
蛋白质二级结构
螺旋结构：
延展结构：
蛋白质超二级结构：
氨基酸
倾向于产生螺旋结构的氨基酸：
倾向于产生延展结构的氨基酸：
倾向于产生无序结构的氨基酸：
无产生任何结构倾向的氨基酸：
细胞膜
其它
细胞内信号
与钙调控
细胞骨架重构蛋白
其它
钙结合蛋白结构域
胞外配体
鈣結合蛋白
 
描述
取自“https://zh.wikipedia.org/w/index.php?title=EF手&oldid=29750239”